Newly discovered regulatory aspects of amino acid metabolism will be studied. This includes an investigation of the mechanism of dehydrogenation of several amino acids (e.g., aspartate, tyrosine, tryptophan, alanine, ornithine, etc.) to their respective keto acids plus ammonia by transaminase-glutamate dehydrogenase enzyme-enzyme complexes. Both the physical structure and the physiological significance of these complexes will be investigated. In addition, the effects of physiologically or pharmacologically significant compounds (e.g., anti- psychotic drugs, etc,) on these enzyme-enzyme complexes will be further investigated. Efforts will be made to identify the keto group on transaminase. Furthermore, the physiological function of this group as well as the nature and function of the DPNH binding site on the transaminase will be explored. The possibility that other physiologically significant enzyme-enzyme complexes are formed will be explored.